A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase

被引:275
作者
Janjusevic, R
Abramovitch, RB
Martin, GB
Stebbins, CE
机构
[1] Cornell Univ, Boyce Thompson Inst Plant Res, Ithaca, NY 14853 USA
[2] Rockefeller Univ, Lab Struct Microbiol, New York, NY 10021 USA
[3] Cornell Univ, Dept Plant Pathol, Ithaca, NY 14853 USA
关键词
D O I
10.1126/science.1120131
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The Pseudomonas syringae protein AvrPtoB is translocated into plant cells, where it inhibits immunity-associated programmed cell. death (PCD). The structure of a C-terminal domain of AvrPtoB that is essential for anti-PCD activity reveals an unexpected homology to the U-box and RING-finger components of eukaryotic E3 ubiquitin ligases, and we show that AvrPtoB has ubiquitin ligase activity. Mutation of conserved residues involved in the binding of E2 ubiquitin-conjugating enzymes abolishes this activity in vitro, as well as anti-PCD activity in tomato leaves, which dramatically decreases virulence. These results show that Pseudomonas syringae uses a mimic of host E3 ubiquitin ligases to inactivate plant defenses.
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页码:222 / 226
页数:5
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